Please use this identifier to cite or link to this item: https://doi.org/10.1002/pmic.200600030
DC FieldValue
dc.titleProteomic analysis of protein profiles during early development of the zebrafish, Danio rerio
dc.contributor.authorTay, T.L.
dc.contributor.authorLin, Q.
dc.contributor.authorSeow, T.K.
dc.contributor.authorTan, K.H.
dc.contributor.authorHew, C.L.
dc.contributor.authorGong, Z.
dc.date.accessioned2014-10-27T08:37:42Z
dc.date.available2014-10-27T08:37:42Z
dc.date.issued2006-05
dc.identifier.citationTay, T.L., Lin, Q., Seow, T.K., Tan, K.H., Hew, C.L., Gong, Z. (2006-05). Proteomic analysis of protein profiles during early development of the zebrafish, Danio rerio. Proteomics 6 (10) : 3176-3188. ScholarBank@NUS Repository. https://doi.org/10.1002/pmic.200600030
dc.identifier.issn16159853
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/101484
dc.description.abstractIn the present study, profiles of protein expression were examined during early development of zebrafish, an increasingly popular experimental model in vertebrate development and human diseases. By 2-DE, an initial increase in protein spots from 6 h post-fertilization (hpf) to 8-10 hpf was observed. There was no dramatic change in protein profiles up to 18 hpf, but significant changes occurred in subsequent stages. Interestingly, 49% of the proteins detected at 6 hpf remained detectable by 1 week of age. To map the protein expression patterns in 2-D gels, MALDI-TOF/TOF MS was employed to identify selected protein spots from early embryos. 108 protein spots were found to match known proteins and they were derived from 55 distinct genes. Interestingly, 11 (20%) of them produced multiple protein isoforms or distinct cleavage products. Although deyolked embryos were used in the analysis, a large number of vitellogenin derivatives remained prominently present in the embryos. Other than these, most of the identified proteins are cytosolic, cytoskeletal and nuclear proteins, which are involved in diversified functions such as metabolism, cytoskeleton, translation, protein degradation, etc. Some of the proteins with interesting temporal expression profiles during development are further discussed. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/pmic.200600030
dc.sourceScopus
dc.subjectEmbryo
dc.subjectHeat shock protein
dc.subjectMass spectrometry
dc.subjectTwo-dimensional gel electrophoresis
dc.subjectVitellogenin
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1002/pmic.200600030
dc.description.sourcetitleProteomics
dc.description.volume6
dc.description.issue10
dc.description.page3176-3188
dc.description.codenPROTC
dc.identifier.isiut000238010400023
Appears in Collections:Staff Publications

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